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蛋白 AMP 化的化学报告器。

A chemical reporter for protein AMPylation.

机构信息

The Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, New York 10065, USA.

出版信息

J Am Chem Soc. 2011 Nov 2;133(43):17103-5. doi: 10.1021/ja205137d. Epub 2011 Oct 7.

Abstract

Protein AMPylation is an emerging post-translational modification, which plays key roles in bacterial pathogenesis and cell biology. Enzymes with AMPylation activity, referred to as AMPylators, have been identified in several bacterial pathogens and eukaryotes. To facilitate the study of this unique modification, we developed an alkynyl chemical reporter for detection and identification of protein AMPylation substrates. Covalent functionalization of AMPylation substrates with the alkynyl reporter in lieu of adenylyl 5'-monophosphate (AMP) allows their subsequent bioorthogonal ligation with azide-fluorescent dyes or affinity enrichment tags. We show that this chemical reporter is transferred by a range of AMPylators onto their cognate protein substrates and allows rapid detection and identification of AMPylated substrates.

摘要

蛋白质 AMP 化是一种新兴的翻译后修饰,在细菌发病机制和细胞生物学中起着关键作用。具有 AMP 化活性的酶,称为 AMP 化酶,已在几种细菌病原体和真核生物中被鉴定。为了促进对这种独特修饰的研究,我们开发了一种炔基化学报告物,用于检测和鉴定蛋白质 AMP 化底物。用炔基报告物取代腺苷酰-5'-单磷酸 (AMP) 对 AMP 化底物进行共价功能化,允许它们随后与叠氮荧光染料或亲和富集标签进行生物正交连接。我们表明,这种化学报告物可被一系列 AMP 化酶转移到其同源蛋白底物上,并允许快速检测和鉴定 AMP 化底物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5534/3246509/3f54c2538b0b/nihms330522f1.jpg

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